Journal
EUKARYOTIC CELL
Volume 8, Issue 12, Pages 1869-1879Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/EC.00218-09
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Funding
- United Kingdom Medical Research Council
- Wellcome Trust Malaria Functional Genomics Initiative [066742]
- European Union
- U.S. National Institutes of Health [HL078826]
- MRC [MC_U117532067] Funding Source: UKRI
- Medical Research Council [MC_U117532067] Funding Source: researchfish
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We have identified a new Plasmodium falciparum erythrocyte binding protein that appears to be located in the micronemes of the merozoite stage of the parasite and membrane linked through a glycosylphosphatidylinositol (GPI) anchor. The protein is designated GPI-anchored micronemal antigen (GAMA) and was identified by applying a set of selection criteria to identify previously uncharacterized merozoite proteins that may have a role in cell invasion. The protein is also present in the proteomes of the sporozoite and ookinete micronemes and is conserved throughout the genus. GAMA contains a novel domain that may be constrained by disulfide bonds and a predicted C-terminal hydrophobic sequence that is presumably replaced by the GPI. The protein is synthesized late during schizogony, processed into two fragments that are linked by a disulfide bond, and translocated to an apical location, which is probably the micronemes. In a proportion of free merozoites GAMA can also be detected on the parasite surface. Following erythrocyte invasion the bulk of the protein is shed in a soluble form, although a short C-terminal fragment may be carried into the newly invaded red blood cell. The protein was shown to bind reversibly to erythrocytes and therefore represents a new example of a host cell binding protein.
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